Recombinant Human Fc gamma RIIB/C (CD32b/c) Protein, CF

1 μg/lane of Recombinant Human Fc gamma RIIB/C (CD32b/c) was resolved with SDS-PAGE under reducing (R) conditions and visualized by silver staining, showing multiple bands at 27-35 kDa.

Recombinant Human Fc gamma RIIB/C (CD32b/c) (Catalog # 1875-CD) binds human IgG with an estimated Kd <200 nM.

• Reactivity: Hu
• Applications: Binding Activity
• Format: Carrier-Free

Recombinant Human Fc gamma RIIB/C (CD32b/c) Protein, CF Summary

• Details of Functionality: Measured by its ability to bind human IgG with an estimated K_d <200 nM.
• Source: Mouse myeloma cell line, NS0-derived human Fc gamma RIIB/C (CD32b/c) protein
  Ala46-Pro217, with a C-terminal 10-His tag
• Accession #: P31994
• N-terminal Sequence: Ala46
• Protein/Peptide Type: Recombinant Proteins
• Gene: FCGR2B
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Endotoxin Note: <1.0 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Binding Activity
• Theoretical MW: 21 kDa.
  Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
• SDS-PAGE: 25-35 kDa, reducing conditions

Packaging, Storage & Formulations

• Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
• Buffer: Lyophilized from a 0.2 μm filtered solution in PBS.
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Reconstitution Instructions: Reconstitute at 100 μg/mL in sterile PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human Fc gamma RIIB/C (CD32b/c) Protein, CF

• Fc gamma RIIB/C (CD32b/c)

Background

Receptors for the Fc region of IgG (Fc gamma Rs) are members of the Ig superfamily that function in the activation or inhibition of immune responses such as degranulation, phagocytosis, ADCC (antibody-dependent cellular toxicity), cytokine release, and B cell proliferation (1-3). The Fc gamma Rs have been divided into three classes based on close relationships in their extracellular domains; these groups are designated Fc gamma  RI (also known as CD64), Fc gamma  RII (CD32), and Fc gamma  RIII (CD16). Each group may be encoded by multiple genes and exist in different isoforms depending on species and cell type. The CD64 proteins are high affinity receptors (~10^-8-10^-9 M) capable of binding monomeric IgG, whereas the CD16 and CD32 proteins bind IgG with lower affinities (~10^-6-10^-7 M) only recognizing IgG aggregates surrounding multivalent antigens (1, 4). Fc gamma Rs that deliver an activating signal either have an intrinsic immunoreceptor tyrosine-based activation motif (ITAM) within their cytoplasmic domains or associate with one of the ITAM-bearing adapter subunits, FcR gamma or zeta (3, 5). The only inhibitory member in human and mouse, Fc gamma  RIIB, has an intrinsic cytoplasmic immunoreceptor tyrosine-based inhibitory motif (ITIM). The coordinated functioning of activating and inhibitory receptors is necessary for successful initiation, amplification, and termination of immune responses (5).

Three distinct genes encode the human CD32 group, and the protein products are designated Fc gamma  RIIA, B, and C (1). These receptors are glycoproteins of approximately 40 kDa having two extracellular Ig-like domains. The Fc gamma  RII proteins share 94-99% amino acid identity in their extracellular domains but differ substantially in their transmembrane and cytoplasmic domains. Fc gamma  RIIA associates with FcR gamma , and delivers an activating signal upon ligand binding (3, 5). In contrast, Fc gamma  RIIB delivers an inhibitory signal. Fc gamma  RIIC represents an unequal cross-over event between the IIA and IIB genes. Its extracellular domain shares 99% amino acid identity with Fc gamma  RIIB, but a portion of the cytoplasmic domain is closely related to Fc gamma  RIIA. Fc gamma  RII proteins are expressed on cells of both myeloid and lymphoid lineages as well as on cells of non-hematopoietic origin.

1. van de Winkel, J. and P. Capes (1993) Immunol. Today 14:215. 
2. Raghaven, M. and P. Bjorkman (1996) Annu. Rev. Cell Dev. Biol. 12:181. 
3. Ravetch, J. and S. Bolland (2001) Annu. Rev. Immunol. 19:275.
4. Takai, T. (2002) Nature Rev. Immunol. 2:580.
5. Ravetch, J. and L. Lanier (2000) Science 290:84.

Publications for Fc gamma RIIB/C (CD32b/c) (1875-CD)(15)

Publications using 1875-CD

• Y Kitanaga, D Yamajuku, S Kubo, K Nakamura, M Maeda, M Seki, Y Kaneko, F Kinugasa, T Morokata, Y Kondo, H Yoshinari, S Nakayamada, T Sumida, Y Tanaka Discovery of a novel Igbeta and FcgammaRIIB cross-linking antibody, ASP2713, and its potential application in the treatment of systemic lupus erythematosus International immunopharmacology, 2021;101(0):108343. 2021 [PMID: 34781122] (ELISA Capture, Human)
• EH Aitken, T Damelang, A Ortega-Paj, A Alemu, W Hasang, S Dini, HW Unger, M Ome-Kaius, MA Nielsen, A Salanti, J Smith, S Kent, PM Hogarth, BD Wines, JA Simpson, A Chung, SJ Rogerson Developing a multivariate prediction model of antibody features associated with protection of malaria-infected pregnant women from placental malaria Elife, 2021;10(0):. 2021 [PMID: 34181872] (Bioassay, Human)
• B Vanhove, O Duvaux, J Rousse, PJ Royer, G Evanno, C Ciron, E Lheriteau, L Vacher, N Gervois, R Oger, Y Jacques, S Conchon, A Salama, R Duchi, I Lagutina, A Perota, P Delahaut, M Ledure, M Paulus, RT So, CK Mok, R Bruzzone, M Bouillet, S Brouard, E Cozzi, C Galli, D Blanchard, JM Bach, JP Soulillou High neutralizing potency of swine glyco-humanized polyclonal antibodies against SARS-CoV-2 European Journal of Immunology, 2021;0(0):. 2021 [PMID: 33576494] (Bioassay, Porcine)
• L Zekri, F Vogt, L Osburg, S Müller, J Kauer, T Manz, M Pflügler, A Maurer, JS Heitmann, I Hagelstein, M Märklin, S Hörner, T Todenhöfer, C Calaminus, A Stenzl, B Pichler, C la Fougère, MA Schneider, HG Rammensee, L Zender, B Sipos, HR Salih, G Jung An IgG-based bispecific antibody for improved dual targeting in PSMA-positive cancer Embo Molecular Medicine, 2020;0(0):e11902. 2020 [PMID: 33372710] (ELISA Capture, Human)
• PA Blundell, D Lu, M Wilkinson, A Dell, S Haslam, RJ Pleass Insertion of N-Terminal Hinge Glycosylation Enhances Interactions of the Fc Region of Human IgG1 Monomers with Glycan-Dependent Receptors and Blocks Hemagglutination by the Influenza Virus J. Immunol., 2019;0(0):. 2019 [PMID: 30683699] (ELISA (Capture), Human)
• F Arce Varga, AJS Furness, K Litchfield, K Joshi, R Rosenthal, E Ghorani, I Solomon, MH Lesko, N Ruef, C Roddie, JY Henry, L Spain, A Ben Aissa, A Georgiou, YNS Wong, M Smith, D Strauss, A Hayes, D Nicol, T O'Brien, L Mårtensson, A Ljungars, I Teige, B Frendéus, , , , M Pule, T Marafioti, M Gore, J Larkin, S Turajlic, C Swanton, KS Peggs, SA Quezada Fc Effector Function Contributes to the Activity of Human Anti-CTLA-4 Antibodies Cancer Cell, 2018;0(0):. 2018 [PMID: 29576375] (Surface Plasmon Resonance (SPR, Human)
• N Seo, A Polozova, M Zhang, Z Yates, S Cao, H Li, S Kuhns, G Maher, HJ McBride, J Liu Analytical and functional similarity of Amgen biosimilar ABP 215 to bevacizumab MAbs, 2018;0(0):1-58. 2018 [PMID: 29553864] (Surface Plasmon Resonance (SPR, Human)
• D Zhang, B Whitaker, MG Derebe, ML Chiu Fc?RII-binding Centyrins mediate agonism and antibody-dependent cellular phagocytosis when fused to an anti-OX40 antibody MAbs, 2018;0(0):1-13. 2018 [PMID: 29359992] (CIS Display, Human)
• S Järnum, A Runström, R Bockermann, L Winstedt, M Crispin, C Kjellman Enzymatic inactivation of endogenous IgG by IdeS enhances�therapeutic antibody efficacy Mol. Cancer Ther., 2017;0(0):. 2017 [PMID: 28533435] (Bioassay, Human)
• Meuris L, Santens F, Elson G, Festjens N, Boone M, Dos Santos A, Devos S, Rousseau F, Plets E, Houthuys E, Malinge P, Magistrelli G, Cons L, Chatel L, Devreese B, Callewaert N GlycoDelete engineering of mammalian cells simplifies N-glycosylation of recombinant proteins. Nat Biotechnol, 2014;32(5):485-9. 2014 [PMID: 24752077] (Bioassay, Human)
• Xie J, Yamniuk A, Borowski V, Kuhn R, Susulic V, Rex-Rabe S, Yang X, Zhou X, Zhang Y, Gillooly K, Brosius R, Ravishankar R, Waggie K, Mink K, Price L, Rehfuss R, Tamura J, An Y, Cheng L, Abramczyk B, Ignatovich O, Drew P, Grant S, Bryson J, Suchard S, Salter-Cid L, Nadler S, Suri A Engineering of a novel anti-CD40L domain antibody for treatment of autoimmune diseases. J Immunol, 2014;192(9):4083-92. 2014 [PMID: 24670803] (Bioassay, Human)
• Derer S, Glorius P, Schlaeth M, Lohse S, Klausz K, Muchhal U, Desjarlais J, Humpe A, Valerius T, Peipp M Increasing FcgammaRIIa affinity of an FcgammaRIII-optimized anti-EGFR antibody restores neutrophil-mediated cytotoxicity. MAbs, 2014;6(2):409-21. 2014 [PMID: 24492248] (Surface Plasmon Resonance, N/A)
• Franco A, Damdinsuren B, Ise T, Dement-Brown J, Li H, Nagata S, Tolnay M Human Fc receptor-like 5 binds intact IgG via mechanisms distinct from those of Fc receptors. J Immunol, 0;190(11):5739-46. 0 [PMID: 23616577] (Surface Plasmon Resonance (SPR, Human)
• Development and characterisation of monoclonal antibodies specific for the murine inhibitory FcgammaRIIB (CD32B). Eur J Immunol, 2012;42(8):2109-20. 2012 [PMID: 22760702] (Surface Plasmon Resonance, N/A)
• Richards JO, Karki S, Lazar GA, Chen H, Dang W, Desjarlais JR Optimization of antibody binding to FcgammaRIIa enhances macrophage phagocytosis of tumor cells. Mol. Cancer Ther., 2008;7(8):2517-27. 2008 [PMID: 18723496] (Surface Plasmon Resonance, Human)

Bioinformatics

• Gene Symbol: FCGR2B
• Uniprot:
  • P31994()